| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-100 |
Sentence |
denotes |
Structural elements in dextran glucosidase responsible for high specificity to long chain substrate. |
| T2 |
101-275 |
Sentence |
denotes |
Dextran glucosidase from Streptococcus mutans (SMDG) and Bacillus oligo-1,6-glucosidases, members of glycoside hydrolase family 13 enzymes, have the high sequence similarity. |
| T3 |
276-390 |
Sentence |
denotes |
Each of them is specific to alpha-1,6-glucosidic linkage at the non-reducing end of substrate to liberate glucose. |
| T4 |
391-560 |
Sentence |
denotes |
The activities toward long isomaltooligosaccharides were different in both enzymes, in which SMDG and oligo-1,6-glucosidase showed high and low activities, respectively. |
| T5 |
561-655 |
Sentence |
denotes |
We determined the structural elements essential for high activity toward long-chain substrate. |
| T6 |
656-903 |
Sentence |
denotes |
From conformational comparison between SMDG and B. cereus oligo-1,6-glucosidase (three-dimensional structure has been solved), Trp238 and short beta-->alpha loop 4 of SMDG were considered to contribute to the high activity to long-chain substrate. |
| T7 |
904-1058 |
Sentence |
denotes |
W238A had similar kcat/Km value for isomaltotriose to that for isomaltose, suggesting that the affinity of subsite +2 was decreased by Trp238 replacement. |
| T8 |
1059-1343 |
Sentence |
denotes |
Trp238 mutants as well as the chimeric enzyme having longer beta-->alpha loop 4 of B. subtilis oligo-1,6-glucosidase showed lower preference for long-chain substrates, indicating that both Trp238 and short beta-->alpha loop 4 were important for high activity to long-chain substrates. |
